2WTL
Crystal structure of BfrA from M. tuberculosis
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | EMBL/DESY, HAMBURG BEAMLINE X11 |
| Synchrotron site | EMBL/DESY, HAMBURG |
| Beamline | X11 |
| Temperature [K] | 295 |
| Detector technology | IMAGE PLATE |
| Detector | MAR555 FLAT PANEL |
| Spacegroup name | I 4 |
| Unit cell lengths | 125.960, 125.960, 175.840 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 36.047 - 2.590 |
| R-factor | 0.1849 |
| Rwork | 0.183 |
| R-free | 0.22830 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3bkn |
| RMSD bond length | 0.016 |
| RMSD bond angle | 2.090 |
| Data reduction software | AUTOMAR |
| Data scaling software | AUTOMAR |
| Phasing software | PHENIX (AUTOMR WIZARD) |
| Refinement software | PHENIX ((PHENIX.REFINE)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 25.000 | 2.590 |
| High resolution limit [Å] | 2.500 | 2.500 |
| Rmerge | 0.100 | 0.290 |
| Number of reflections | 45901 | |
| <I/σ(I)> | 6.7 | 1.6 |
| Completeness [%] | 99.4 | 97.1 |
| Redundancy | 4.4 | 4.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 8 | PROTEIN (9MG/ML) WAS CRYSTALLIZED WITH 1.6M NACL; 100MM TRIS-HCL, PH 8.0 AT ROOM TEMPERATURE |
